ID W2SD30_9EURO Unreviewed; 575 AA.
AC W2SD30;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Malic enzyme {ECO:0000256|RuleBase:RU003426};
GN ORFNames=HMPREF1541_00089 {ECO:0000313|EMBL:ETN45908.1};
OS Cyphellophora europaea CBS 101466.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN45908.1, ECO:0000313|Proteomes:UP000030752};
RN [1] {ECO:0000313|EMBL:ETN45908.1, ECO:0000313|Proteomes:UP000030752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN45908.1,
RC ECO:0000313|Proteomes:UP000030752};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phialophora europaea CBS 101466.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000256|PIRSR:PIRSR000106-3};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003426}.
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DR EMBL; KB822711; ETN45908.1; -; Genomic_DNA.
DR RefSeq; XP_008710620.1; XM_008712398.1.
DR AlphaFoldDB; W2SD30; -.
DR STRING; 1220924.W2SD30; -.
DR GeneID; 19967428; -.
DR VEuPathDB; FungiDB:HMPREF1541_00089; -.
DR eggNOG; KOG1257; Eukaryota.
DR HOGENOM; CLU_011405_5_2_1; -.
DR InParanoid; W2SD30; -.
DR OrthoDB; 1069499at2759; -.
DR Proteomes; UP000030752; Unassembled WGS sequence.
DR GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR CDD; cd05312; NAD_bind_1_malic_enz; 1.
DR Gene3D; 3.40.50.10380; Malic enzyme, N-terminal domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR015884; Malic_enzyme_CS.
DR InterPro; IPR012301; Malic_N_dom.
DR InterPro; IPR037062; Malic_N_dom_sf.
DR InterPro; IPR012302; Malic_NAD-bd.
DR InterPro; IPR001891; Malic_OxRdtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR PANTHER; PTHR23406:SF32; NAD-DEPENDENT MALIC ENZYME, MITOCHONDRIAL; 1.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR PIRSF; PIRSF000106; ME; 1.
DR PRINTS; PR00072; MALOXRDTASE.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000106-3};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003426};
KW Reference proteome {ECO:0000313|Proteomes:UP000030752}.
FT DOMAIN 88..273
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 283..539
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 111
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 187
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 258
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 259
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 282
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 426
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 470
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 575 AA; 63583 MW; A98C2D44679C6FF1 CRC64;
MTSDSKFNGL PLWKDKPVKT KLSGRLLLDT PFLNKGTCFT HEERHEFGLH GLLPTNVQNI
DQQVARAYQQ YSSLPDDLAK NNFMTSMAGQ NSVLYYRLIL DHITEMFSII YTPTEGDAIE
NYSRIFRRPE GCFLPIGHVD EVEERMSKFV VPDQDGNGVD YIVVSDGEEI LGIGDQGIGG
ILISTAKLAL TTACAGIHPN RTLPVVLDTG TNNEELLEDD LYLGIKHPRV RGEKYDELVE
NFINTANKLF PNAYIHFEDF GVTNARRLLD RYRKRTACFN DDIQGTGCVT LAAIMAALKI
SKLKLTDMRM VVFGSGSAGC GIAEQVQSAI AAEANKSKDE VKRNIWCVDR DGLILDQMDL
SIAQKPFARA ASEWSGKDTK SLQAIIAEVK PHVLIGTSTK PGAFTQEVVE EMARHVERPV
IFPLSNPTRL HEAQPSDINK WTKGKALIAT GSPFPPVEFE GNKYEVAECN NSVCFPGIGL
GAVLSRAKLL TDKMLAEGVR ALADASPALK DANKGLVPDV DQARPVSVKI AMAVIRAAQD
EGLARTSHIP ESDEELEQWV KAQMWEPTYK RYEKV
//
